| Literature DB >> 30762928 |
Chengmin Xuan1, Yong Gao2, Mingwei Jin1, Shumei Xu1, Lei Wang1, Yuan Wang1, Rui Han1, Kunpeng Shi1, Xincheng Chen3, Qi An1.
Abstract
The ubiquitin-proteasome system is the primary cellular pathway for protein degradation, mediating 80% of intracellular protein degradation. Because of the widespread presence of ubiquitin-modified protein substrates, ubiquitination can regulate a variety of cellular activities including cell proliferation, apoptosis, autophagy, endocytosis, DNA damage repair, and immune responses. With the continuous generation of genomics data in recent years it has become particularly important to analyze these data effectively and reasonably. Cacybp forms a complex with the E3 ubiquitinated ligase Siah1 to participate in ubiquitination. We analyzed Cacybp-associated genes using the Gene Expression Omnibus (GEO) and CGGA (Chinese Glioma Genome Atlas) databases and identified 121 differentially expressed genes (DEGs), of which 46 were downregulated and 75 were upregulated. The biological processes, molecular functions, and protein-protein interaction (PPI) network of differential genes were analyzed by Cytoscape software and STRING software. We found no difference in Cacybp expression among different grades of gliomas and there was no significant association between the expression level of Cacybp and the prognosis of patients with glioma in LGG and GBM.Entities:
Keywords: Cacybp; bioinformatics; differentially expressed gene; glioma; protein-protein interaction; ubiquitination
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Year: 2019 PMID: 30762928 DOI: 10.1002/iub.1999
Source DB: PubMed Journal: IUBMB Life ISSN: 1521-6543 Impact factor: 3.885